EF1A_CAEEL
ID EF1A_CAEEL Reviewed; 463 AA.
AC P53013;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Elongation factor 1-alpha;
DE Short=EF-1-alpha;
GN Name=eft-3; ORFNames=F31E3.5;
GN and
GN Name=eft-4; ORFNames=R03G5.1;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (EFT-3 AND EFT-4).
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}.
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DR EMBL; FO080948; CCD68024.1; -; Genomic_DNA.
DR EMBL; FO080392; CCD63407.1; -; Genomic_DNA.
DR PIR; T16218; T16218.
DR RefSeq; NP_498520.1; NM_066119.6.
DR RefSeq; NP_509323.1; NM_076922.4.
DR AlphaFoldDB; P53013; -.
DR SMR; P53013; -.
DR BioGRID; 41189; 22.
DR BioGRID; 45968; 4.
DR DIP; DIP-26595N; -.
DR IntAct; P53013; 5.
DR STRING; 6239.F31E3.5.1; -.
DR iPTMnet; P53013; -.
DR EPD; P53013; -.
DR PaxDb; P53013; -.
DR PeptideAtlas; P53013; -.
DR EnsemblMetazoa; F31E3.5.1; F31E3.5.1; WBGene00001168.
DR EnsemblMetazoa; R03G5.1.1; R03G5.1.1; WBGene00001169.
DR EnsemblMetazoa; R03G5.1.2; R03G5.1.2; WBGene00001169.
DR EnsemblMetazoa; R03G5.1.3; R03G5.1.3; WBGene00001169.
DR GeneID; 175975; -.
DR GeneID; 181044; -.
DR KEGG; cel:CELE_F31E3.5; -.
DR KEGG; cel:CELE_R03G5.1; -.
DR UCSC; F31E3.5.2; c. elegans.
DR CTD; 175975; -.
DR CTD; 181044; -.
DR WormBase; F31E3.5; CE01270; WBGene00001168; eft-3.
DR WormBase; R03G5.1a; CE01270; WBGene00001169; eft-4.
DR eggNOG; KOG0052; Eukaryota.
DR GeneTree; ENSGT00940000164334; -.
DR HOGENOM; CLU_007265_3_5_1; -.
DR InParanoid; P53013; -.
DR OMA; AIRDMGM; -.
DR OrthoDB; 1150082at2759; -.
DR PhylomeDB; P53013; -.
DR Reactome; R-CEL-3371511; HSF1 activation.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-8876725; Protein methylation.
DR SignaLink; P53013; -.
DR PRO; PR:P53013; -.
DR Proteomes; UP000001940; Chromosome III.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00001168; Expressed in adult organism and 5 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IDA:WormBase.
DR GO; GO:0003746; F:translation elongation factor activity; IBA:GO_Central.
DR GO; GO:0008135; F:translation factor activity, RNA binding; ISS:WormBase.
DR GO; GO:0006412; P:translation; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc.
DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF03143; GTP_EFTU_D3; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00483; EF-1_alpha; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Phosphoprotein; Protein biosynthesis; Reference proteome.
FT CHAIN 1..463
FT /note="Elongation factor 1-alpha"
FT /id="PRO_0000090918"
FT DOMAIN 5..242
FT /note="tr-type G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 14..21
FT /note="G1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 70..74
FT /note="G2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 91..94
FT /note="G3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 153..156
FT /note="G4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 194..196
FT /note="G5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059"
FT REGION 443..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 14..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 91..95
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 153..156
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT MOD_RES 301
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
FT MOD_RES 374
FT /note="5-glutamyl glycerylphosphorylethanolamine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 463 AA; 50668 MW; 12544AF1F17E15B7 CRC64;
MGKEKVHINI VVIGHVDSGK STTTGHLIYK CGGIDKRTIE KFEKEAQEMG KGSFKYAWVL
DKLKAERERG ITIDIALWKF ETAKYYITII DAPGHRDFIK NMITGTSQAD CAVLVVACGT
GEFEAGISKN GQTREHALLA QTLGVKQLIV ACNKMDSTEP PFSEARFTEI TNEVSGFIKK
IGYNPKAVPF VPISGFNGDN MLEVSSNMPW FKGWAVERKE GNASGKTLLE ALDSIIPPQR
PTDRPLRLPL QDVYKIGGIG TVPVGRVETG IIKPGMVVTF APQNVTTEVK SVEMHHESLP
EAVPGDNVGF NVKNVSVKDI RRGSVCSDSK QDPAKEARTF HAQVIIMNHP GQISNGYTPV
LDCHTAHIAC KFNELKEKVD RRTGKKVEDF PKFLKSGDAG IVELIPTKPL CVESFTDYAP
LGRFAVRDMR QTVAVGVIKS VEKSDGSSGK VTKSAQKAAP KKK
